Ribosome articles within Nature Communications

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  • Article
    | Open Access

    Ribosome biogenesis in eukaryotes is a complex process that involves more than 200 protein factors. Here the authors present a structural analysis of a collection of human pre-60S structures sampled through a nuclear export adaptor NMD3, representing structural snapshots of pre-60S particles immediately before and after passing through nuclear pore complex.

    • Xiaomeng Liang
    • , Mei-Qing Zuo
    •  & Ning Gao

  • Article
    | Open Access

    Translation within mitochondria relies upon specialized mitoribosomes and initiation factors. Here the authors use Cryo-EM and single molecule approaches to describe the early steps leading to translation initiation in human mitochondria, and the roles of mitochondria-specific ribosomal proteins and initiation factors mtIF2 and mtIF3.

    • Anas Khawaja
    • , Yuzuru Itoh
    •  & Joanna Rorbach

  • Article
    | Open Access

    Ribosomes of all organisms have retained 5S rRNA as an autonomous rRNA species. Here the authors engineer a bacterial strain with ribosomes that do not have free 5S rRNA, and carry structural analyses that suggest the evolutionary preservation of 5S rRNA as an independent molecule is based on its role in the dynamic process of ribosome biogenesis.

    • Shijie Huang
    • , Nikolay A. Aleksashin
    •  & Alexander S. Mankin

  • Article
    | Open Access

    Ribosome engineering is an emerging powerful approach for synthetic protein synthesis. Here the authors invert the Ribo-T system, using the engineered ribosome to translate the proteome while the native ribosome translates specific mRNA.

    • Nikolay A. Aleksashin
    • , Teresa Szal
    •  & Alexander S. Mankin

  • Article
    | Open Access

    Upon transition to stationary phase or upon stress, bacteria limit protein synthesis through small inhibitory proteins that bind the ribosome. Here the authors decipher the interaction mode of the bacterial ribosome silencing factor (RsfS) at atomic details to provide an in depth view of how it shutdowns ribosomes.

    • Iskander Khusainov
    • , Bulat Fatkhullin
    •  & Marat Yusupov

  • Article
    | Open Access

    Directed evolution of the ribosome is challenging because the requirement of cell viability limits the mutations that can be made. Here the authors develop a platform for in vitro ribosome synthesis and evolution (RISE) to overcome these constraints.

    • Michael J. Hammerling
    • , Brian R. Fritz
    •  & Michael C. Jewett

  • Article
    | Open Access

    The ErbB3 receptor binding protein Ebp1 binds to ribosomes and is linked to translational control. Here, the authors present the cryo-EM structure of human Ebp1 bound to a non-translating 80S ribosome and find that Ebp1 blocks the tunnel exit and recruits the rRNA expansion segment ES27L to the tunnel exit.

    • Klemens Wild
    • , Milan Aleksić
    •  & Irmgard Sinning

  • Article
    | Open Access

    In bacteria, the conserved trans-translation system serves as the primary pathway of ribosome rescue, but many species can also use alternative rescue pathways. Here the authors report that in B. subtilis, the rescue factor BrfA binds to non-stop stalled ribosomes, recruits RF2 but not RF1, and induces transition of the ribosome into an open active conformation.

    • Naomi Shimokawa-Chiba
    • , Claudia Müller
    •  & Shinobu Chiba

  • Article
    | Open Access

    Ribo-T is a tethered ribosome complex capable of orthogonal ribosome-mRNA functionality, but has low activity. Here the authors evolve new tether designs that support faster growth and increased protein expression.

    • Erik D. Carlson
    • , Anne E. d’Aquino
    •  & Michael C. Jewett

  • Article
    | Open Access

    MazF endoribonucleases are thought to arrest growth of Mycobacterium tuberculosis by global translation inhibition. Here, Barth et al. show that MazF-mt9 cleaves a specific tRNA, leading to ribosome stalling at AAA codons and thus selective mRNA degradation and changes in transcriptome and proteome.

    • Valdir C. Barth
    • , Ju-Mei Zeng
    •  & Nancy A. Woychik

  • Article
    | Open Access

    Metal ions play essential roles in myriads of biological processes, from catalytic co-factors to supporting protein and nucleic acid structures. Here the authors use long-wavelength X-ray diffraction to locate hundreds of potassium ions taking part in the formation of rRNA tertiary structure, mediating rRNA–protein interactions and supporting ribosomal protein structures and function.

    • Alexey Rozov
    • , Iskander Khusainov
    •  & Gulnara Yusupova

  • Article
    | Open Access

    Genes encoding protein complex subunits are often dispersed in the genome of eukaryotes, raising the question how these protein complexes assemble. Here, the authors provide evidence that mammalian nuclear transcription complexes are formed co-translationally to ensure specific and functional interactions.

    • Ivanka Kamenova
    • , Pooja Mukherjee
    •  & László Tora

  • Article
    | Open Access

    In eukaryotes, ribosome biogenesis culminates in the cytoplasm with the maturation of the peptidyl transfer center (PTC). Here the authors describe several structures of intermediates in late nuclear and cytoplasmic maturation of the large ribosomal subunit that reveal the tightly-choreographed sequence of protein and RNA rearrangements that lead to the completion of the PTC.

    • Yi Zhou
    • , Sharmishtha Musalgaonkar
    •  & David W. Taylor

  • Article
    | Open Access

    The tethered ribosome system Ribo-T supports cell proliferation though at a reduced rate. Here the authors show this is due to slower ribosome assembly instead of reduced functionality.

    • Nikolay A. Aleksashin
    • , Margus Leppik
    •  & Alexander S. Mankin

  • Article
    | Open Access

    Viruses can encode genes that regulate the host's translational machinery to their advantage. Here, the authors show that viruses encode ribosomal proteins that can be incorporated into the host’s ribosome and may affect translation.

    • Carolina M. Mizuno
    • , Charlotte Guyomar
    •  & Mart Krupovic

  • Article
    | Open Access

    Rix7 is a type II AAA-ATPase that is required for the assembly of the large ribosomal subunit. Here the authors present the 4.5 Å cryo-EM structure of the Rix7 homohexamer with a polypeptide fragment bound in its central channel and provide insights into the function of Rix7 as a molecular unfoldase.

    • Yu-Hua Lo
    • , Mack Sobhany
    •  & Robin E. Stanley

  • Article
    | Open Access

    Microorganisms must regulate allocation of resources in nutrient-limited conditions. Here, the authors combine Ribo-seq, RNA-seq and TSS-seq to study resource allocation in the acetogen C. ljungdahlii, and show that dynamic regulation of translational efficiency of metabolic pathways is critical.

    • Mahmoud M. Al-Bassam
    • , Ji-Nu Kim
    •  & Karsten Zengler

  • Article
    | Open Access

    During stress conditions bacterial ribosomes dimerize and form inactive but stable hibernating 100S particles, a process that is facilitated by the hibernation-promoting factor (HPF). Here the authors analyze 100S dimer formation as a function of HPF protein concentration and present the Thermus thermophilus 100S ribosome cryo-EM structure.

    • Rasmus Kock Flygaard
    • , Niels Boegholm
    •  & Lasse B. Jenner

  • Article
    | Open Access

    Competition between synthetic genetic circuits and host genes for shared resources can complicate circuit design and lead to failure. Here the authors demonstrate, mathematically and experimentally, the use of orthogonal ribosomes to decouple competing genes.

    • Alexander P. S. Darlington
    • , Juhyun Kim
    •  & Declan G. Bates

  • Article
    | Open Access

    Repeat-associated non-AUG (RAN) translation contributes to the pathogenic mechanism of several microsatellite expansion diseases. Here the authors delineate the different steps involved in recruiting the ribosome to initiate G4C2 RAN translation to produce poly-Glycine Alanine, poly-Glycine Proline, and poly-Glycine Arginine repeats.

    • Ricardos Tabet
    • , Laure Schaeffer
    •  & Clotilde Lagier-Tourenne

  • Article
    | Open Access

    Excision of internal transcribed spacer 2 (ITS2) within eukaryotic pre-ribosomal RNA is essential for ribosome function. Here, the authors reconstitute the entire cycle of ITS2 processing in vitro using purified components, providing insights into the cleavage process and demonstrating that 26S pre-rRNA processing necessarily precedes 7S pre-rRNA processing.

    • Lisa Fromm
    • , Sebastian Falk
    •  & Ed Hurt

  • Article
    | Open Access

    Leishmaniasis is a parasitic disease transmitted by the bite of infected sand flies. Here the authors describe an atomic resolution cryo-EM structure of the Leishmania ribosome in complex with the recently approved drug paromomycin (PAR) and highlight conserved elements in the drug binding pocket that mediate PAR deleterious effects on the parasite.

    • Moran Shalev-Benami
    • , Yan Zhang
    •  & Georgios Skiniotis

  • Article
    | Open Access

    The GTP-bound form of initiation factor 2 (IF2) promotes translation initiation by accelerating 50S ribosomal subunit joining the 30S ribosomal initiation complex (30S IC). Here the authors use single-molecule FRET and ensemble rapid kinetic methods to uncover the mechanism behind IF2-mediated subunit joining.

    • Kelvin Caban
    • , Michael Pavlov
    •  & Ruben L. Gonzalez Jr

  • Article
    | Open Access

    The eukaryotic release factor eRF1 is able to recognize the three stop codons UAA, UAG and UGA with high accuracy, while discriminating against near-cognate codons. Here the authors use molecular dynamic simulation to provide insight into the molecular basis behind the remarkable codon specificity of eRF1.

    • Christoffer Lind
    • , Ana Oliveira
    •  & Johan Åqvist

  • Article
    | Open Access

    The yeast Hsp70 homolog Ssb is a chaperone that binds translating ribosomes where it is thought to function primarily by promoting nascent peptide folding. Here the authors find that the ribosome biogenesis defect associated with the loss of Ssb is attributable to a specific disruption in TORC1 signaling rather than defects in ribosomal protein folding.

    • Kaivalya Mudholkar
    • , Edith Fitzke
    •  & Sabine Rospert

  • Article
    | Open Access

    Ribosome biogenesis is a dynamic process that involves the ordered assembly of ribosomal proteins and numerous RNA structural rearrangements. Here the authors apply ChemModSeq, a high-throughput RNA structure probing method, to quantitatively measure changes in RNA flexibility during the nucleolar stages of 60S assembly in yeast.

    • Elena Burlacu
    • , Fredrik Lackmann
    •  & Sander Granneman

  • Article
    | Open Access

    When bacteria enter the stationary growth phase, protein translation is suppressed via the dimerization of 70S ribosomes into inactive complexes. Here the authors provide a structural basis for how the dual domain hibernation promotion factor promotes ribosome dimerization and hibernation in bacteria.

    • Linda E. Franken
    • , Gert T. Oostergetel
    •  & Albert Guskov

  • Article
    | Open Access

    Under conditions of nutrient limitation, bacterial ribosomes undergo dimerization, forming a 100S complex that is translationally inactive. Here the authors present the structural basis for formation of the 100S complexes in Gram-positive bacteria, shedding light on the mechanism of translation suppression by the ribosome-silencing factors.

    • Donna Matzov
    • , Shintaro Aibara
    •  & Ada E. Yonath

  • Article
    | Open Access

    The transcription factor Gcn4 is known to regulate yeast amino acid synthesis. Here, the authors show that Gcn4 also acts as a repressor of protein biosynthesis in a range of conditions that enhance yeast lifespan, such as ribosomal protein knockout, calorie restriction or mTOR inhibition.

    • Nitish Mittal
    • , Joao C. Guimaraes
    •  & Mihaela Zavolan

  • Article
    | Open Access

    Several protein quality control mechanisms are in place to trigger the rapid degradation of aberrant polypeptides and mRNAs. Here the authors describe a mechanism of ribosome-mediated quality control that involves the ubiquitination of ribosomal proteins by the E3 ubiquitin ligase Hel2/RQT1.

    • Yoshitaka Matsuo
    • , Ken Ikeuchi
    •  & Toshifumi Inada

  • Article
    | Open Access

    Programmed −1 ribosomal frameshifting (−1 PRF) is a mechanism whereby specific signals within mRNAs direct ribosomes to shift into an alternative reading frame. Here the authors describe a mechanism of −1 PRF that is temporally regulated by a viral protein over the course of the virus replicative cycle.

    • Sawsan Napthine
    • , Roger Ling
    •  & Andrew E. Firth

  • Article
    | Open Access

    Membrane proteins are inserted co-transnationally through the association between ribosome, the signal recognition particle and its receptor, and the membrane-bound translocon. Here the authors present a cryo-EM reconstruction of this quaternary complex in the activated state and propose a model for signal sequence transfer to the translocon.

    • Ahmad Jomaa
    • , Yu-Hsien Hwang Fu
    •  & Nenad Ban

  • Article
    | Open Access

    PTEN is a potent tumour suppressor involved in cell growth, proliferation and survival. Here the authors identify an N-terminal extended isoform of PTEN, termed PTENβ that negatively regulates ribosomal DNA transcription and cell proliferation, expanding the pleiotropic functions of the PTEN family.

    • Hui Liang
    • , Xi Chen
    •  & Yuxin Yin

  • Article
    | Open Access

    Translocation of the tRNA on the ribosome is associated with large-scale molecular movements of the ribosomal L1 stalk. Here the authors identify the key determinants that allow these dramatic movements, and suggest they represent general strategies used to enable large-scale motions in functional RNAs.

    • Srividya Mohan
    •  & Harry F Noller

  • Article
    | Open Access

    Nonsense-mediated mRNA decay (NMD) is a quality control pathway that recognizes and degrades transcripts harbouring nonsense mutations. Here the authors show that the ATPase activity of UPF1 mediates functional interactions between the NMD machinery and ribosomes required for efficient ribosome release at premature termination codons.

    • Lucas D. Serdar
    • , DaJuan L. Whiteside
    •  & Kristian E. Baker

  • Article
    | Open Access

    mRNA surveillance is essential to maintain homeostasis in eukaryotes and is activated by mRNAs lacking a stop codon. Here the authors describe a high resolution cryo-EM structure of a nonstop complex that shows how arrested ribosome recognition is achieved during Dom34-mediated mRNA surveillance.

    • Tarek Hilal
    • , Hiroshi Yamamoto
    •  & Christian M.T. Spahn

  • Article
    | Open Access

    The correct folding of proteins often requires the intervention molecular chaperones, which can occur co-translationally. Here the authors identify elements of yeast Ssb (Hsp70) that mediate ribosomal binding, and suggest a mechanism that directs efficient interaction of Ssb with the nascent chain.

    • Marie A. Hanebuth
    • , Roman Kityk
    •  & Elke Deuerling

  • Article
    | Open Access

    Epithelial-to-mesenchymal transition is a key process in tumorigenesis but little is known about the molecular mechanism regulating such process at the translational level. Here, the authors identify a subset of mRNAs important for this process that are specifically modulated by the RNA-binding protein CELF1.

    • Arindam Chaudhury
    • , Shebna Cheema
    •  & Joel R. Neilson

  • Article
    | Open Access

    Ribosome recycling orchestrated by ABCE1 connects translation termination and mRNA surveillance mechanisms with re-initiation. Using a cross-linking and mass spectrometry approach, Kiosze-Becker et al. provide new information on the large conformational rearrangements that occur during ribosome recycling.

    • Kristin Kiosze-Becker
    • , Alessandro Ori
    •  & Robert Tampé

  • Article
    | Open Access

    Initiation factor eIF2, common to eukaryotes and archaea, is a central actor in translation initiation. Here the authors describe two cryo-EM structures of archaeal 30S initiation complexes that provide a novel view of the central role that e/aIF2 plays in start codon selection.

    • Pierre-Damien Coureux
    • , Christine Lazennec-Schurdevin
    •  & Yves Mechulam

  • Article
    | Open Access

    The translation of mRNA by the ribosome is governed by a series of large-scale conformational transitions. Here the authors use MD simulations to demonstrate how the rate of dissociation of elongation factor Tu affects the dynamics of tRNA accommodation and proofreading.

    • Jeffrey K. Noel
    •  & Paul C. Whitford

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